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UniProtKB/Swiss-Prot Q99732: Variant p.Gly112Ser

Lipopolysaccharide-induced tumor necrosis factor-alpha factor
Gene: LITAF
Variant information

Variant position:  112
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LP/P [Disclaimer]
The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change:  From Glycine (G) to Serine (S) at position 112 (G112S, p.Gly112Ser).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Change from glycine (G) to small size and polar (S)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  0
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description:  In CMT1C; does not abolish interaction with NEDD4 and TSG101.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  112
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  161
The length of the canonical sequence.

Location on the sequence:   IQMCCPSCNKMIVSQLSYNA  G ALTWLSCGSLCLLGCIAGCC
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.

Residue conservation: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         IQMCCPSCNKMIVSQLSYNAGALTWLSCGSLCLLGCIAGCC

Mouse                         VQMCCPSCSKMIVTQLSYNAGALTWLSCGSLCLLGCVAGCC

Rat                           IQMCCPSCNKMIVTQLSYNAGALTWLSCGSLCLLGCVAGCC

Chicken                       VQMSCPSCNQMIVTRLCYESGALTWLSCGGLFLLGCIAGCC

Xenopus tropicalis            VQMCCRSCNSMITTRLEYSSGALAWLSCGGLCLLGCIGGCC

Zebrafish                     VQAHCPVCSQSVITRLEYSSGPLVWLSCAGLAVFGCIYGCC

Sequence annotation in neighborhood:  
The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.

TypePositionsDescription
Chain 1 – 161 Lipopolysaccharide-induced tumor necrosis factor-alpha factor
Domain 76 – 160 LITAF
Region 111 – 134 Membrane-binding amphipathic helix
Metal binding 96 – 96 Zinc
Metal binding 99 – 99 Zinc
Mutagenesis 96 – 96 C -> A. Abolishes association with cytoplasmic vesicle membranes.


Literature citations

SIMPLE interacts with NEDD4 and TSG101: evidence for a role in lysosomal sorting and implications for Charcot-Marie-Tooth disease.
Shirk A.J.; Anderson S.K.; Hashemi S.H.; Chance P.F.; Bennett C.L.;
J. Neurosci. Res. 82:43-50(2005)
Cited for: INTERACTION WITH NEDD4 AND TSG101; CHARACTERIZATION OF VARIANTS CMT1C SER-112; ASN-115 AND GLY-116; MUTAGENESIS OF 17-PRO--ALA-19 AND TYR-23;

Mutation of a putative protein degradation gene LITAF/SIMPLE in Charcot-Marie-Tooth disease 1C.
Street V.A.; Bennett C.L.; Goldy J.D.; Shirk A.J.; Kleopa K.A.; Tempel B.L.; Lipe H.P.; Scherer S.S.; Bird T.D.; Chance P.F.;
Neurology 60:22-26(2003)
Cited for: VARIANTS CMT1C SER-112; ASN-115 AND GLY-116;

Early onset neuropathy in a compound form of Charcot-Marie-Tooth disease.
Meggouh F.; de Visser M.; Arts W.F.M.; De Coo R.I.F.M.; van Schaik I.N.; Baas F.;
Ann. Neurol. 57:589-591(2005)
Cited for: VARIANT CMT1C SER-112; VARIANT VAL-92;

SIMPLE mutations in Charcot-Marie-Tooth disease and the potential role of its protein product in protein degradation.
Saifi G.M.; Szigeti K.; Wiszniewski W.; Shy M.E.; Krajewski K.; Hausmanowa-Petrusewicz I.; Kochanski A.; Reeser S.; Mancias P.; Butler I.; Lupski J.R.;
Hum. Mutat. 25:372-383(2005)
Cited for: VARIANTS CMT1C MET-49; SER-112 AND VAL-122; VARIANT VAL-92; PUTATIVE FUNCTION;

Application of whole exome sequencing in undiagnosed inherited polyneuropathies.
Klein C.J.; Middha S.; Duan X.; Wu Y.; Litchy W.J.; Gu W.; Dyck P.J.; Gavrilova R.H.; Smith D.I.; Kocher J.P.; Dyck P.J.;
J. Neurol. Neurosurg. Psych. 85:1265-1272(2014)
Cited for: VARIANT CMT1C SER-112;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.